位置:首页 > 蛋白库 > KCD15_MOUSE
KCD15_MOUSE
ID   KCD15_MOUSE             Reviewed;         283 AA.
AC   Q8K0E1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=BTB/POZ domain-containing protein KCTD15;
DE   AltName: Full=Potassium channel tetramerization domain-containing protein 15;
GN   Name=Kctd15;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic breast;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-38, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=25187989; DOI=10.1371/journal.pgen.1004499;
RA   Williams M.J., Goergen P., Rajendran J., Zheleznyakova G., Haegglund M.G.,
RA   Perland E., Bagchi S., Kalogeropoulou A., Khan Z., Fredriksson R.,
RA   Schioeth H.B.;
RT   "Obesity-linked homologues TfAP-2 and Twz establish meal frequency in
RT   Drosophila melanogaster.";
RL   PLoS Genet. 10:e1004499-e1004499(2014).
CC   -!- FUNCTION: During embryonic development, interferes with neural crest
CC       formation. Inhibits AP2 transcriptional activity by interaction with
CC       its activation domain (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TFAP2A; this interaction inhibits TFAP2A
CC       transcriptional activation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25187989}. Note=In
CC       the brain, localizes to the arcuate hypothalamic nucleus, the
CC       ventromedial hypothalamic nucleus and the accumbens nucleus of the
CC       ventral striatum. {ECO:0000269|PubMed:25187989}.
CC   -!- TISSUE SPECIFICITY: Localizes to neurons in areas of the cerebral
CC       cortex, cerebellum and hypothalamus (at protein level).
CC       {ECO:0000269|PubMed:25187989}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK034731; BAC28810.1; -; mRNA.
DR   EMBL; BC031749; AAH31749.1; -; mRNA.
DR   CCDS; CCDS21141.1; -.
DR   RefSeq; NP_666300.1; NM_146188.1.
DR   RefSeq; XP_006539963.1; XM_006539900.1.
DR   RefSeq; XP_006539964.1; XM_006539901.3.
DR   RefSeq; XP_006539965.1; XM_006539902.3.
DR   RefSeq; XP_006539966.1; XM_006539903.3.
DR   RefSeq; XP_006539967.1; XM_006539904.3.
DR   RefSeq; XP_006539968.1; XM_006539905.1.
DR   AlphaFoldDB; Q8K0E1; -.
DR   SMR; Q8K0E1; -.
DR   IntAct; Q8K0E1; 1.
DR   STRING; 10090.ENSMUSP00000103705; -.
DR   iPTMnet; Q8K0E1; -.
DR   PhosphoSitePlus; Q8K0E1; -.
DR   MaxQB; Q8K0E1; -.
DR   PaxDb; Q8K0E1; -.
DR   PeptideAtlas; Q8K0E1; -.
DR   PRIDE; Q8K0E1; -.
DR   ProteomicsDB; 301758; -.
DR   Antibodypedia; 29083; 256 antibodies from 29 providers.
DR   DNASU; 233107; -.
DR   Ensembl; ENSMUST00000032709; ENSMUSP00000032709; ENSMUSG00000030499.
DR   Ensembl; ENSMUST00000108069; ENSMUSP00000103704; ENSMUSG00000030499.
DR   Ensembl; ENSMUST00000108070; ENSMUSP00000103705; ENSMUSG00000030499.
DR   GeneID; 233107; -.
DR   KEGG; mmu:233107; -.
DR   UCSC; uc009gjf.2; mouse.
DR   CTD; 79047; -.
DR   MGI; MGI:2385276; Kctd15.
DR   VEuPathDB; HostDB:ENSMUSG00000030499; -.
DR   eggNOG; KOG2723; Eukaryota.
DR   GeneTree; ENSGT00940000159496; -.
DR   HOGENOM; CLU_061268_1_0_1; -.
DR   InParanoid; Q8K0E1; -.
DR   OMA; CREDRRM; -.
DR   OrthoDB; 971350at2759; -.
DR   PhylomeDB; Q8K0E1; -.
DR   TreeFam; TF315332; -.
DR   BioGRID-ORCS; 233107; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Kctd15; mouse.
DR   PRO; PR:Q8K0E1; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q8K0E1; protein.
DR   Bgee; ENSMUSG00000030499; Expressed in ear vesicle and 215 other tissues.
DR   ExpressionAtlas; Q8K0E1; baseline and differential.
DR   Genevisible; Q8K0E1; MM.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   CDD; cd18388; BTB_POZ_KCTD15; 1.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR045904; KCTD15_T1-type_BTB.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR003131; T1-type_BTB.
DR   Pfam; PF02214; BTB_2; 1.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..283
FT                   /note="BTB/POZ domain-containing protein KCTD15"
FT                   /id="PRO_0000247252"
FT   DOMAIN          56..126
FT                   /note="BTB"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96SI1"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15345747,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   283 AA;  31886 MW;  7D67029CD51B8E2B CRC64;
     MPHRKERPSG SSLNAHGSSG TAEGGNMSRL SLTRSPVSPL AAQGIPLPAQ LTKANAPVHI
     DVGGHMYTSS LATLTKYPDS RISRLFNGTE PIVLDSLKQH YFIDRDGEIF RYILSFLRTS
     KLLLPDDFKD FNLLYEEARY YQLQPMVREL ERWQQDQEQR RRSRACDCLV VRVTPDLGER
     IALSGEKALI EEVFPETGDV MCNSVNAGWN QDPTHVIRFP LNGYCRLNSV QVLERLFQRG
     FSVAASCGGG VDSSQFSEYV LCREERRPQP TPTAVRIKQE PLD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024